Evidence map›Paper›PMID 20363749›Full record

ArticleThe Journal of biological chemistry2010

The angiogenic inhibitor long pentraxin PTX3 forms an asymmetric octamer with two binding sites for FGF2.

Antonio Inforzato, Clair Baldock, Thomas A Jowitt, David F Holmes, Ragnar Lindstedt, Marcella Marcellini, Vincenzo Rivieccio, David C Briggs, Karl E Kadler, Antonio Verdoliva and 4 more

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 62 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed, 1 pooled it
3.3field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

62 citing papers in PubMed, 1 synthesis or guideline pooled it, 112 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Role of long pentraxin PTX3 in cancer.Clinical and experimental medicine · 2023
    Review
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2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 2 countries.

Antonio InforzatoWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, United Kingdom.
Clair Baldock
Thomas A Jowitt
David F Holmes
Ragnar Lindstedt
Marcella Marcellini
Vincenzo Rivieccio
David C Briggs
Karl E Kadler
Antonio Verdoliva
Barbara Bottazzi
Alberto Mantovani
Giovanni Salvatori
Anthony J Day
University of Manchester · GBSigma Tau (Italy) · ITWellcome Centre for Cell-Matrix Research · GBFondazione Humanitas per la Ricerca · IT

Funding

Arthritis Research UK 16539Medical Research Council G0701180
6 · The paper itself

Abstract

The inflammation-associated long pentraxin PTX3 plays key roles in innate immunity, female fertility, and vascular biology (e.g. it inhibits FGF2 (fibroblast growth factor 2)-mediated angiogenesis). PTX3 is composed of multiple protomers, each composed of distinct N- and C-terminal domains; however, it is not known how these are organized or contribute to its functional properties. Here, biophysical analyses reveal that PTX3 is composed of eight identical protomers, associated through disulfide bonds, forming an elongated and asymmetric, molecule with two differently sized domains interconnected by a stalk. The N-terminal region of the protomer provides the main structural determinant underlying this quaternary organization, supporting formation of a disulfide-linked tetramer and a dimer of dimers (a non-covalent tetramer), giving rise to the asymmetry of the molecule. Furthermore, the PTX3 octamer is shown to contain two FGF2 binding sites, where it is the tetramers that act as the functional units in ligand recognition. Thus, these studies provide a unifying model of the PTX3 oligomer, explaining both its quaternary organization and how this is required for its antiangiogenic function.

Indexed as

Neovascularization, PathologicAngiogenesis InhibitorsAnimalsBinding SitesCHO CellsC-Reactive ProteinCricetinaeCricetulusDisulfidesFibroblast Growth Factor 2HumansLigandsPentraxinsProtein BindingProtein Structure, TertiaryRecombinant ProteinsAngiogenesis InhibitorsC-Reactive ProteinDisulfidesFibroblast Growth Factor 2LigandsPentraxinsRecombinant ProteinsSerum Amyloid P-Component

Identifiers

PMID20363749
PMCPMC2878532
OpenAlexW2006877316

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.